Further studies of tyrosine surrogates in opioid receptor peptide ligands
A series of opioid peptide ligands containing modified N-terminal tyrosine (Tyr) residues was prepared and evaluated against cloned human μ, δ, and κ opioid receptors. This work extends the recent discovery that ( S)-4-carboxamidophenylalanine (Cpa) is an effective tyrosine bioisostere. Amino acids...
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| Veröffentlicht in: | Bioorganic & medicinal chemistry letters 2007-05, Vol.17 (9), p.2656-2660 |
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| container_title | Bioorganic & medicinal chemistry letters |
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| creator | Dolle, Roland E. Michaut, Mathieu Martinez-Teipel, Blanca Belanger, Serge Graczyk, Thomas M. DeHaven, Robert N. |
| description | A series of opioid peptide ligands containing modified N-terminal tyrosine (Tyr) residues was prepared and evaluated against cloned human μ, δ, and κ opioid receptors. This work extends the recent discovery that (
S)-4-carboxamidophenylalanine (Cpa) is an effective tyrosine bioisostere. Amino acids containing negatively charged functional groups in place of tyrosine’s phenolic hydroxyl lacked receptor affinity, while exchange of Tyr for (
S)-4-aminophenylalanine was modestly successful. Peptides containing the new amino acids, (
S)-4-carboxamido-2,6-dimethylphenylalanine (Cdp) and (
S)-β-(2-aminobenzo[
d]thiazol-6-yl)alanine (Aba), displayed binding (
K
i) and functional (EC
50) profiles comparable to the parent ligands at the three receptors. Cdp represents the best performing Tyr surrogate in terms of overall activity, while Cpa and Aba show a subtle proclivity toward the δ receptor. |
| doi_str_mv | 10.1016/j.bmcl.2007.01.092 |
| format | Article |
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S)-4-carboxamidophenylalanine (Cpa) is an effective tyrosine bioisostere. Amino acids containing negatively charged functional groups in place of tyrosine’s phenolic hydroxyl lacked receptor affinity, while exchange of Tyr for (
S)-4-aminophenylalanine was modestly successful. Peptides containing the new amino acids, (
S)-4-carboxamido-2,6-dimethylphenylalanine (Cdp) and (
S)-β-(2-aminobenzo[
d]thiazol-6-yl)alanine (Aba), displayed binding (
K
i) and functional (EC
50) profiles comparable to the parent ligands at the three receptors. Cdp represents the best performing Tyr surrogate in terms of overall activity, while Cpa and Aba show a subtle proclivity toward the δ receptor.</description><identifier>ISSN: 0960-894X</identifier><identifier>EISSN: 1464-3405</identifier><identifier>DOI: 10.1016/j.bmcl.2007.01.092</identifier><identifier>PMID: 17350835</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Bioisostere ; Biological and medical sciences ; Chemistry, Pharmaceutical - methods ; Cloning, Molecular ; Drug Design ; Humans ; Hydrogen Bonding ; Kinetics ; Ligands ; Medical sciences ; Models, Chemical ; Molecular Conformation ; Neuropharmacology ; Neurotransmitters. Neurotransmission. Receptors ; Opioid ; Peptidergic system (neuropeptide, opioid peptide, opiates...). Adenosinergic and purinergic systems ; Peptides ; Peptides - chemistry ; Pharmacology. Drug treatments ; Receptors, Opioid - chemistry ; Receptors, Opioid, delta - chemistry ; Receptors, Opioid, kappa - chemistry ; Receptors, Opioid, mu - chemistry ; Tyrosine - chemistry ; Tyrosine mimetic ; Tyrosine surrogate</subject><ispartof>Bioorganic & medicinal chemistry letters, 2007-05, Vol.17 (9), p.2656-2660</ispartof><rights>2007 Elsevier Ltd</rights><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c415t-89450e66adad80040054ef006af24a8a4a00966dd8ca824c7312de1248a8a7b63</citedby><cites>FETCH-LOGICAL-c415t-89450e66adad80040054ef006af24a8a4a00966dd8ca824c7312de1248a8a7b63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bmcl.2007.01.092$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18676958$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17350835$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dolle, Roland E.</creatorcontrib><creatorcontrib>Michaut, Mathieu</creatorcontrib><creatorcontrib>Martinez-Teipel, Blanca</creatorcontrib><creatorcontrib>Belanger, Serge</creatorcontrib><creatorcontrib>Graczyk, Thomas M.</creatorcontrib><creatorcontrib>DeHaven, Robert N.</creatorcontrib><title>Further studies of tyrosine surrogates in opioid receptor peptide ligands</title><title>Bioorganic & medicinal chemistry letters</title><addtitle>Bioorg Med Chem Lett</addtitle><description>A series of opioid peptide ligands containing modified N-terminal tyrosine (Tyr) residues was prepared and evaluated against cloned human μ, δ, and κ opioid receptors. This work extends the recent discovery that (
S)-4-carboxamidophenylalanine (Cpa) is an effective tyrosine bioisostere. Amino acids containing negatively charged functional groups in place of tyrosine’s phenolic hydroxyl lacked receptor affinity, while exchange of Tyr for (
S)-4-aminophenylalanine was modestly successful. Peptides containing the new amino acids, (
S)-4-carboxamido-2,6-dimethylphenylalanine (Cdp) and (
S)-β-(2-aminobenzo[
d]thiazol-6-yl)alanine (Aba), displayed binding (
K
i) and functional (EC
50) profiles comparable to the parent ligands at the three receptors. Cdp represents the best performing Tyr surrogate in terms of overall activity, while Cpa and Aba show a subtle proclivity toward the δ receptor.</description><subject>Bioisostere</subject><subject>Biological and medical sciences</subject><subject>Chemistry, Pharmaceutical - methods</subject><subject>Cloning, Molecular</subject><subject>Drug Design</subject><subject>Humans</subject><subject>Hydrogen Bonding</subject><subject>Kinetics</subject><subject>Ligands</subject><subject>Medical sciences</subject><subject>Models, Chemical</subject><subject>Molecular Conformation</subject><subject>Neuropharmacology</subject><subject>Neurotransmitters. Neurotransmission. Receptors</subject><subject>Opioid</subject><subject>Peptidergic system (neuropeptide, opioid peptide, opiates...). Adenosinergic and purinergic systems</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Pharmacology. Drug treatments</subject><subject>Receptors, Opioid - chemistry</subject><subject>Receptors, Opioid, delta - chemistry</subject><subject>Receptors, Opioid, kappa - chemistry</subject><subject>Receptors, Opioid, mu - chemistry</subject><subject>Tyrosine - chemistry</subject><subject>Tyrosine mimetic</subject><subject>Tyrosine surrogate</subject><issn>0960-894X</issn><issn>1464-3405</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LxDAQhoMouq7-AQ_Si962TtokTcGLiF-w4EXBW8gmU83SbWrSCv57U3bBm54Gkmde3nkIOaOQU6Diap2vNqbNC4AqB5pDXeyRGWWCLUoGfJ_MoBawkDV7OyLHMa4BKAPGDskRrUoOsuQz8nQ_huEDQxaH0TqMmW-y4Tv46DrM4hiCf9dDenZd5nvnnc0CGuwHH7I-DWcxa9277mw8IQeNbiOe7uacvN7fvdw-LpbPD0-3N8uFYZQPUx0OKIS22koABsAZNgBCNwXTUjMNqbawVhotC2aqkhYWacFk-qxWopyTy21uH_zniHFQGxcNtq3u0I9RVVAKKoH_C9KaU0brKbHYgibdHQM2qg9uo8O3oqAm02qtJtNqMq2AqmQ6LZ3v0sfVBu3vyk5tAi52gI5Gt03QnXHxl5OiEjWXibvecpikfTkMKhqHnUHrkupBWe_-6vEDsficDw</recordid><startdate>20070501</startdate><enddate>20070501</enddate><creator>Dolle, Roland E.</creator><creator>Michaut, Mathieu</creator><creator>Martinez-Teipel, Blanca</creator><creator>Belanger, Serge</creator><creator>Graczyk, Thomas M.</creator><creator>DeHaven, Robert N.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20070501</creationdate><title>Further studies of tyrosine surrogates in opioid receptor peptide ligands</title><author>Dolle, Roland E. ; Michaut, Mathieu ; Martinez-Teipel, Blanca ; Belanger, Serge ; Graczyk, Thomas M. ; DeHaven, Robert N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-89450e66adad80040054ef006af24a8a4a00966dd8ca824c7312de1248a8a7b63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Bioisostere</topic><topic>Biological and medical sciences</topic><topic>Chemistry, Pharmaceutical - methods</topic><topic>Cloning, Molecular</topic><topic>Drug Design</topic><topic>Humans</topic><topic>Hydrogen Bonding</topic><topic>Kinetics</topic><topic>Ligands</topic><topic>Medical sciences</topic><topic>Models, Chemical</topic><topic>Molecular Conformation</topic><topic>Neuropharmacology</topic><topic>Neurotransmitters. Neurotransmission. Receptors</topic><topic>Opioid</topic><topic>Peptidergic system (neuropeptide, opioid peptide, opiates...). Adenosinergic and purinergic systems</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>Pharmacology. Drug treatments</topic><topic>Receptors, Opioid - chemistry</topic><topic>Receptors, Opioid, delta - chemistry</topic><topic>Receptors, Opioid, kappa - chemistry</topic><topic>Receptors, Opioid, mu - chemistry</topic><topic>Tyrosine - chemistry</topic><topic>Tyrosine mimetic</topic><topic>Tyrosine surrogate</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dolle, Roland E.</creatorcontrib><creatorcontrib>Michaut, Mathieu</creatorcontrib><creatorcontrib>Martinez-Teipel, Blanca</creatorcontrib><creatorcontrib>Belanger, Serge</creatorcontrib><creatorcontrib>Graczyk, Thomas M.</creatorcontrib><creatorcontrib>DeHaven, Robert N.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Bioorganic & medicinal chemistry letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dolle, Roland E.</au><au>Michaut, Mathieu</au><au>Martinez-Teipel, Blanca</au><au>Belanger, Serge</au><au>Graczyk, Thomas M.</au><au>DeHaven, Robert N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Further studies of tyrosine surrogates in opioid receptor peptide ligands</atitle><jtitle>Bioorganic & medicinal chemistry letters</jtitle><addtitle>Bioorg Med Chem Lett</addtitle><date>2007-05-01</date><risdate>2007</risdate><volume>17</volume><issue>9</issue><spage>2656</spage><epage>2660</epage><pages>2656-2660</pages><issn>0960-894X</issn><eissn>1464-3405</eissn><abstract>A series of opioid peptide ligands containing modified N-terminal tyrosine (Tyr) residues was prepared and evaluated against cloned human μ, δ, and κ opioid receptors. This work extends the recent discovery that (
S)-4-carboxamidophenylalanine (Cpa) is an effective tyrosine bioisostere. Amino acids containing negatively charged functional groups in place of tyrosine’s phenolic hydroxyl lacked receptor affinity, while exchange of Tyr for (
S)-4-aminophenylalanine was modestly successful. Peptides containing the new amino acids, (
S)-4-carboxamido-2,6-dimethylphenylalanine (Cdp) and (
S)-β-(2-aminobenzo[
d]thiazol-6-yl)alanine (Aba), displayed binding (
K
i) and functional (EC
50) profiles comparable to the parent ligands at the three receptors. Cdp represents the best performing Tyr surrogate in terms of overall activity, while Cpa and Aba show a subtle proclivity toward the δ receptor.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>17350835</pmid><doi>10.1016/j.bmcl.2007.01.092</doi><tpages>5</tpages></addata></record> |
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| ispartof | Bioorganic & medicinal chemistry letters, 2007-05, Vol.17 (9), p.2656-2660 |
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| subjects | Bioisostere Biological and medical sciences Chemistry, Pharmaceutical - methods Cloning, Molecular Drug Design Humans Hydrogen Bonding Kinetics Ligands Medical sciences Models, Chemical Molecular Conformation Neuropharmacology Neurotransmitters. Neurotransmission. Receptors Opioid Peptidergic system (neuropeptide, opioid peptide, opiates...). Adenosinergic and purinergic systems Peptides Peptides - chemistry Pharmacology. Drug treatments Receptors, Opioid - chemistry Receptors, Opioid, delta - chemistry Receptors, Opioid, kappa - chemistry Receptors, Opioid, mu - chemistry Tyrosine - chemistry Tyrosine mimetic Tyrosine surrogate |
| title | Further studies of tyrosine surrogates in opioid receptor peptide ligands |
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